|Reactivity||Human, Mouse, Rat|
|Calculated MW||17303 Da|
|Other Names||Stathmin, Leukemia-associated phosphoprotein p18, Metablastin, Oncoprotein 18, Op18, Phosphoprotein p19, pp19, Prosolin, Protein Pr22, pp17, STMN1, C1orf215, LAP18, OP18|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding Serine 24 of human Op18 was used as an immunogen. This antibody detects Op18 phosphorylated at Serine 24.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Op18 Antibody Phospho (pS24) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||C1orf215, LAP18, OP18|
|Function||Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser- 16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear (By similarity).|
|Cellular Location||Cytoplasm, cytoskeleton.|
|Tissue Location||Ubiquitous. Expression is strongest in fetal and adult brain, spinal cord, and cerebellum, followed by thymus, bone marrow, testis, and fetal liver. Expression is intermediate in colon, ovary, placenta, uterus, and trachea, and is readily detected at substantially lower levels in all other tissues examined. Lowest expression is found in adult liver. Present in much greater abundance in cells from patients with acute leukemia of different subtypes than in normal peripheral blood lymphocytes, non-leukemic proliferating lymphoid cells, bone marrow cells, or cells from patients with chronic lymphoid or myeloid leukemia|
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Oncoprotein 18 (Op18) is a proliferation-related cytosolic phosphoprotein which is induced in normal lymphocytes following mitogenic stimulation. Studies of Op18 are of particular interest because of the proposed role it plays in signal transduction and because of its occurrence in markedly increased amounts in acute leukemia cells (1). Oncoprotein 18 has been independently identified due to its increased phosphorylation in response to external signals and its up-regulated expression in acute leukemia. Findings suggest that Op18 may be a physiological substrate for several members of the cdc2 kinase family during both the S-phase and the mitotic phase of the cell cycle (2). Also, findings show that Op18 by itself can fold into a flexible and extended alpha-helix, which is in equilibrium with a less ordered structure. In complex with tubulin, however, all except the last seven C-terminal residues of Op18 are tightly bound to tubulin. Studies suggest results suggest that besides sequestering tubulin, the structural features of Op18 enable the protein specifically to recognize microtubule ends to trigger catastrophes (3).
1. Melhem RF, et al. J Biol Chem 266(27):17747-53, 1991
2. Brattsand G, et al. Eur J Biochem 220(2):359-68, 1994
3. Steinmetz MO, et al. EMBO J 19(4):572-80, 2000
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